A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanism
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference12 articles.
1. THE DENATURATION OF COVALENTLY INHIBITED SWINE PEPSIN
2. Kinetic studies on the unfolding and refolding of pepsinogen in urea. The nature of the rate-limiting step.
3. Nonlinear Regression With Linear Constraints: An Extension of the Magnified Diagonal Method
4. Studies on secondary structure in chicken egg-white lysozyme after reductive cleavage of disulfide bonds
5. The Stability of Globular Protein
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2. Correlating Structure and Activity of Pepsin Enzyme in H2O and D2O for The Study of Gastric Digestion;2022-11-08
3. Foldase and inhibitor functionalities of the pepsinogen prosegment are encoded within discrete segments of the 44 residue domain;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2015-10
4. Effect of the C-terminal Truncation on the Functional Cycle of Chaperonin GroEL;Journal of Biological Chemistry;2008-08
5. Comparison of Solution Structures and Stabilities of Native, Partially Unfolded and Partially Refolded Pepsin;Biochemistry;2006-11-01
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